CREB-binding protein

CREB-binding protein
CREB binding protein

PDB rendering based on 1f81.
External IDs OMIM600140 MGI1098280 HomoloGene68393 GeneCards: CREBBP Gene
EC number
RNA expression pattern
PBB GE CREBBP 202160 at tn.png
PBB GE CREBBP 211808 s at tn.png
More reference expression data
Species Human Mouse
Entrez 1387 12914
Ensembl ENSG00000005339 ENSMUSG00000022521
UniProt Q92793 P45481
RefSeq (mRNA) NM_001079846.1 NM_001025432.1
RefSeq (protein) NP_001073315.1 NP_001020603.1
Location (UCSC) Chr 16:
3.78 – 3.93 Mb
Chr 16:
4.08 – 4.21 Mb
PubMed search [1] [2]

CREB-binding protein, also known as CREBBP or CBP, is a protein that in humans is encoded by the CREBBP gene.[1][2] The CREB protein carries out its function by activating transcription, where interaction with transcription factors is managed by one or more of p300 domains: the nuclear receptor interaction domain (RID), the CREB and MYB interaction domain (KIX), the cysteine/histidine regions (TAZ1/CH1 and TAZ2/CH3) and the interferon response binding domain (IBiD). The CREB protein domains, KIX, TAZ1 and TAZ2, each bind tightly to a sequence spanning both transactivation domains 9aaTADs of transcription factor p53.[3][4]



This gene is ubiquitously expressed and is involved in the transcriptional coactivation of many different transcription factors. First isolated as a nuclear protein that binds to cAMP-response element-binding protein (CREB), this gene is now known to play critical roles in embryonic development, growth control, and homeostasis by coupling chromatin remodeling to transcription factor recognition. The protein encoded by this gene has intrinsic histone acetyltransferase activity and also acts as a scaffold to stabilize additional protein interactions with the transcription complex. This protein acetylates both histone and non-histone proteins. This protein shares regions of very high-sequence similarity with protein EP300 in its bromodomain, cysteine-histidine-rich regions, and histone acetyltransferase domain.[5] Recent results suggest that novel CBP-mediated post-translational N-glycosylation activity alters the conformation of CBP-interacting proteins, leading to regulation of gene expression, cell growth and differentiation,[6]

Clinical significance

Mutations in this gene cause Rubinstein-Taybi syndrome (RTS).[7] Chromosomal translocations involving this gene have been associated with acute myeloid leukemia.[5][8]


CREB-binding protein has been shown to interact with:


  1. ^ Chrivia JC, Kwok RP, Lamb N, Hagiwara M, Montminy MR, Goodman RH (October 1993). "Phosphorylated CREB binds specifically to the nuclear protein CBP". Nature 365 (6449): 855–9. Bibcode 1993Natur.365..855C. doi:10.1038/365855a0. PMID 8413673. 
  2. ^ Wydner KL, Bhattacharya S, Eckner R, Lawrence JB, Livingston DM (November 1995). "Localization of human CREB-binding protein gene (CREBBP) to 16p13.2-p13.3 by fluorescence in situ hybridization". Genomics 30 (2): 395–6. PMID 8586450. 
  3. ^ Teufel DP, Freund SM, Bycroft M, Fersht AR (April 2007). "Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53". PNAS 104 (17): 7009–7014. doi:10.1073/pnas.0702010104. PMC 1855428. PMID 17438265. ; Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M (June 2007). "Nine-amino-acid transactivation domain: establishment and prediction utilities". Genomics 89 (6): 756–68. doi:10.1016/j.ygeno.2007.02.003. PMID 17467953. ; Piskacek M (2009-11-05). "9aaTAD is a common transactivation domain recruits multiple general coactivators TAF9, MED15, CBP/p300 and GCN5". Nature Precedings Pre-publication. doi:10.1038/npre.2009.3488.2. ; Piskacek M (2009-11-05). "9aaTADs mimic DNA to interact with a pseudo-DNA Binding Domain KIX of Med15 (Molecular Chameleons)". Nature Precedings Pre-publication. doi:10.1038/npre.2009.3939.1. ; Piskacek M; Piskacek, Martin (2009-11-20). "9aaTAD Prediction result (2006)". Nature Precedings Pre-publication. doi:10.1038/npre.2009.3984.1. 
  4. ^ The prediction for 9aaTADs (for both acidic and hydrophilic transactivation domains) is available online from ExPASy and EMBnet Spain
  5. ^ a b "Entrez Gene: CREBBP (CREB-binding protein)". 
  6. ^ a b Siddique H, Rao VN, Reddy ES (Aug 2009). "CBP-mediated post-translational N-glycosylation of BRCA2". Int J Oncol. 35 (2): 16387–91. PMID 19578754. 
  7. ^ Petrij F, Giles RH, Dauwerse HG, Saris JJ, Hennekam RC, Masuno M, Tommerup N, van Ommen GJ, Goodman RH, Peters DJ (July 1995). "Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP". Nature 376 (6538): 348–51. Bibcode 1995Natur.376..348P. doi:10.1038/376348a0. PMID 7630403. 
  8. ^ Vizmanos JL, Larráyoz MJ, Lahortiga I, Floristán F, Alvarez C, Odero MD, Novo FJ, Calasanz MJ (April 2003). "t(10;16)(q22;p13) and MORF-CREBBP fusion is a recurrent event in acute myeloid leukemia". Genes Chromosomes Cancer 36 (4): 402–5. doi:10.1002/gcc.10174. PMID 12619164. 
  9. ^ a b c Sano, Y; Tokitou F, Dai P, Maekawa T, Yamamoto T, Ishii S (Oct. 1998). "CBP alleviates the intramolecular inhibition of ATF-2 function". J. Biol. Chem. (UNITED STATES) 273 (44): 29098–105. doi:10.1074/jbc.273.44.29098. ISSN 0021-9258. PMID 9786917. 
  10. ^ a b Kim, J; Jia L, Stallcup M R, Coetzee G A (Feb. 2005). "The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus". J. Mol. Endocrinol. (England) 34 (1): 107–18. doi:10.1677/jme.1.01701. ISSN 0952-5041. PMID 15691881. 
  11. ^ Frønsdal, K; Engedal N, Slagsvold T, Saatcioglu F (Nov. 1998). "CREB binding protein is a coactivator for the androgen receptor and mediates cross-talk with AP-1". J. Biol. Chem. (UNITED STATES) 273 (48): 31853–9. doi:10.1074/jbc.273.48.31853. ISSN 0021-9258. PMID 9822653. 
  12. ^ Ishitani, Ken; Yoshida Tasuku, Kitagawa Hirochika, Ohta Hiroaki, Nozawa Shiro, Kato Shigeaki (Jul. 2003). "p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor". Biochem. Biophys. Res. Commun. (United States) 306 (3): 660–5. doi:10.1016/S0006-291X(03)01021-0. ISSN 0006-291X. PMID 12810069. 
  13. ^ a b Aarnisalo, P; Palvimo J J, Jänne O A (Mar. 1998). "CREB-binding protein in androgen receptor-mediated signaling". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (5): 2122–7. Bibcode 1998PNAS...95.2122A. doi:10.1073/pnas.95.5.2122. ISSN 0027-8424. PMC 19270. PMID 9482849. 
  14. ^ Pitkänen, J; Doucas V, Sternsdorf T, Nakajima T, Aratani S, Jensen K, Will H, Vähämurto P, Ollila J, Vihinen M, Scott H S, Antonarakis S E, Kudoh J, Shimizu N, Krohn K, Peterson P (Jun. 2000). "The autoimmune regulator protein has transcriptional transactivating properties and interacts with the common coactivator CREB-binding protein". J. Biol. Chem. (UNITED STATES) 275 (22): 16802–9. doi:10.1074/jbc.M908944199. ISSN 0021-9258. PMID 10748110. 
  15. ^ Iioka, Takashi; Furukawa Keizo, Yamaguchi Akira, Shindo Hiroyuki, Yamashita Shunichi, Tsukazaki Tomoo (Aug. 2003). "P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain". J. Bone Miner. Res. (United States) 18 (8): 1419–29. doi:10.1359/jbmr.2003.18.8.1419. ISSN 0884-0431. PMID 12929931. 
  16. ^ a b c Fan, Saijun; Ma Yong Xian, Wang Chenguang, Yuan Ren-Qi, Meng Qinghui, Wang Ji-An, Erdos Michael, Goldberg Itzhak D, Webb Paul, Kushner Peter J, Pestell Richard G, Rosen Eliot M (Jan. 2002). "p300 Modulates the BRCA1 inhibition of estrogen receptor activity". Cancer Res. (United States) 62 (1): 141–51. ISSN 0008-5472. PMID 11782371. 
  17. ^ Pao, G M; Janknecht R, Ruffner H, Hunter T, Verma I M (Feb. 2000). "CBP/p300 interact with and function as transcriptional coactivators of BRCA1". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (3): 1020–5. Bibcode 2000PNAS...97.1020P. doi:10.1073/pnas.97.3.1020. ISSN 0027-8424. PMC 15508. PMID 10655477. 
  18. ^ Chai, Y L; Cui J, Shao N, Shyam E, Reddy P, Rao V N (Jan. 1999). "The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter". Oncogene (ENGLAND) 18 (1): 263–8. doi:10.1038/sj.onc.1202323. ISSN 0950-9232. PMID 9926942. 
  19. ^ Benezra, Miriam; Chevallier Nathalie, Morrison Debra J, MacLachlan Timothy K, El-Deiry Wafik S, Licht Jonathan D (Jul. 2003). "BRCA1 augments transcription by the NF-kappaB transcription factor by binding to the Rel domain of the p65/RelA subunit". J. Biol. Chem. (United States) 278 (29): 26333–41. doi:10.1074/jbc.M303076200. ISSN 0021-9258. PMID 12700228. 
  20. ^ a b Neish, A S; Anderson S F, Schlegel B P, Wei W, Parvin J D (Feb. 1998). "Factors associated with the mammalian RNA polymerase II holoenzyme". Nucleic Acids Res. (ENGLAND) 26 (3): 847–53. doi:10.1093/nar/26.3.847. ISSN 0305-1048. PMC 147327. PMID 9443979. 
  21. ^ Kawabuchi, M; Satomi Y, Takao T, Shimonishi Y, Nada S, Nagai K, Tarakhovsky A, Okada M (Apr. 2000). "Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases". Nature (ENGLAND) 404 (6781): 999–1003. doi:10.1038/35010121. ISSN 0028-0836. PMID 10801129. 
  22. ^ a b Yamaguchi, Y; Wada T, Suzuki F, Takagi T, Hasegawa J, Handa H (Aug. 1998). "Casein kinase II interacts with the bZIP domains of several transcription factors". Nucleic Acids Res. (ENGLAND) 26 (16): 3854–61. doi:10.1093/nar/26.16.3854. ISSN 0305-1048. PMC 147779. PMID 9685505. 
  23. ^ Kovacs KA, Steinmann M; Magistretti PJ, Halfon O, Cardinaux JR (Sept. 2003). "CCAAT/enhancer-binding protein family members recruit the coactivator CREB-binding protein and trigger its phosphorylation". J Biol. Chem. (UNITED STATES) 278 (38): 36959–65. doi:10.1074/jbc.M303147200. ISSN 0021-9258. PMID 12857754. 
  24. ^ Lorentz, O; Suh E R, Taylor J K, Boudreau F, Traber P G (Mar. 1999). "CREB-binding [corrected] protein interacts with the homeodomain protein Cdx2 and enhances transcriptional activity". J. Biol. Chem. (UNITED STATES) 274 (11): 7196–9. doi:10.1074/jbc.274.11.7196. ISSN 0021-9258. PMID 10066780. 
  25. ^ Shi, Yuling; Venkataraman Sujatha L, Dodson Gerald E, Mabb Angela M, LeBlanc Scott, Tibbetts Randal S (Apr. 2004). "Direct regulation of CREB transcriptional activity by ATM in response to genotoxic stress". Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (16): 5898–903. Bibcode 2004PNAS..101.5898S. doi:10.1073/pnas.0307718101. ISSN 0027-8424. PMC 395895. PMID 15073328. 
  26. ^ Shimomura, A; Ogawa Y, Kitani T, Fujisawa H, Hagiwara M (Jul. 1996). "Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein". J. Biol. Chem. (UNITED STATES) 271 (30): 17957–60. doi:10.1074/jbc.271.30.17957. ISSN 0021-9258. PMID 8663317. 
  27. ^ Radhakrishnan, I; Pérez-Alvarado G C, Parker D, Dyson H J, Montminy M R, Wright P E (Dec. 1997). "Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions". Cell (UNITED STATES) 91 (6): 741–52. doi:10.1016/S0092-8674(00)80463-8. ISSN 0092-8674. PMID 9413984. 
  28. ^ a b Zor, Tsaffrir; Mayr Bernhard M, Dyson H Jane, Montminy Marc R, Wright Peter E (Nov. 2002). "Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators". J. Biol. Chem. (United States) 277 (44): 42241–8. doi:10.1074/jbc.M207361200. ISSN 0021-9258. PMID 12196545. 
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  30. ^ a b Zhang, Q; Vo N, Goodman R H (Jul. 2000). "Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB". Mol. Cell. Biol. (UNITED STATES) 20 (14): 4970–8. doi:10.1128/MCB.20.14.4970-4978.2000. ISSN 0270-7306. PMC 85947. PMID 10866654. 
  31. ^ a b Ernst, P; Wang J, Huang M, Goodman R H, Korsmeyer S J (Apr. 2001). "MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein". Mol. Cell. Biol. (United States) 21 (7): 2249–58. doi:10.1128/MCB.21.7.2249-2258.2001. ISSN 0270-7306. PMC 86859. PMID 11259575. 
  32. ^ Ledo, Fran; Kremer Leonor, Mellström Britt, Naranjo Jose R (Sep. 2002). "Ca2+-dependent block of CREB-CBP transcription by repressor DREAM". EMBO J. (England) 21 (17): 4583–92. doi:10.1093/emboj/cdf440. ISSN 0261-4189. PMC 126180. PMID 12198160. 
  33. ^ Li, S; Aufiero B, Schiltz R L, Walsh M J (Jun. 2000). "Regulation of the homeodomain CCAAT displacement/cut protein function by histone acetyltransferases p300/CREB-binding protein (CBP)-associated factor and CBP". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (13): 7166–71. Bibcode 2000PNAS...97.7166L. doi:10.1073/pnas.130028697. ISSN 0027-8424. PMC 16517. PMID 10852958. 
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  35. ^ Zhao, Fang; McCarrick-Walmsley Ruth, Akerblad Peter, Sigvardsson Mikael, Kadesch Tom (Jun. 2003). "Inhibition of p300/CBP by early B-cell factor". Mol. Cell. Biol. (United States) 23 (11): 3837–46. doi:10.1128/MCB.23.11.3837-3846.2003. ISSN 0270-7306. PMC 155219. PMID 12748286. 
  36. ^ a b Sheppard, H M; Harries J C, Hussain S, Bevan C, Heery D M (Jan. 2001). "Analysis of the steroid receptor coactivator 1 (SRC1)-CREB binding protein interaction interface and its importance for the function of SRC1". Mol. Cell. Biol. (UNITED STATES) 21 (1): 39–50. doi:10.1128/MCB.21.1.39-50.2001. ISSN 0270-7306. PMC 86566. PMID 11113179. 
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  41. ^ Yoshida, E; Aratani S, Itou H, Miyagishi M, Takiguchi M, Osumu T, Murakami K, Fukamizu A (Dec. 1997). "Functional association between CBP and HNF4 in trans-activation". Biochem. Biophys. Res. Commun. (UNITED STATES) 241 (3): 664–9. doi:10.1006/bbrc.1997.7871. ISSN 0006-291X. PMID 9434765. 
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Further reading

  • Goldman PS, Tran VK, Goodman RH (1997). "The multifunctional role of the co-activator CBP in transcriptional regulation.". Recent Prog. Horm. Res. 52: 103–19; discussion 119–20. PMID 9238849. 
  • Marcello A, Zoppé M, Giacca M (2002). "Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator.". IUBMB Life 51 (3): 175–81. doi:10.1080/152165401753544241. PMID 11547919. 
  • Matt T (2002). "Transcriptional control of the inflammatory response: a role for the CREB-binding protein (CBP).". Acta Med. Austriaca 29 (3): 77–9. doi:10.1046/j.1563-2571.2002.02010.x. PMID 12168567. 
  • Combes R, Balls M, Bansil L, et al. (2002). "An assessment of progress in the use of alternatives in toxicity testing since the publication of the report of the second FRAME Toxicity Committee (1991).". Alternatives to laboratory animals : ATLA 30 (4): 365–406. PMID 12234245. 
  • Minghetti L, Visentin S, Patrizio M, et al. (2004). "Multiple actions of the human immunodeficiency virus type-1 Tat protein on microglial cell functions.". Neurochem. Res. 29 (5): 965–78. doi:10.1023/B:NERE.0000021241.90133.89. PMID 15139295. 
  • Kino T, Pavlakis GN (2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1.". DNA Cell Biol. 23 (4): 193–205. doi:10.1089/104454904773819789. PMID 15142377. 
  • Greene WC, Chen LF (2004). "Regulation of NF-kappaB action by reversible acetylation.". Novartis Found. Symp. 259: 208–17; discussion 218–25. doi:10.1002/0470862637.ch15. PMID 15171256. 
  • Liou LY, Herrmann CH, Rice AP (2005). "HIV-1 infection and regulation of Tat function in macrophages.". Int. J. Biochem. Cell Biol. 36 (9): 1767–75. doi:10.1016/j.biocel.2004.02.018. PMID 15183343. 
  • Pugliese A, Vidotto V, Beltramo T, et al. (2005). "A review of HIV-1 Tat protein biological effects.". Cell Biochem. Funct. 23 (4): 223–7. doi:10.1002/cbf.1147. PMID 15473004. 
  • Bannwarth S, Gatignol A (2005). "HIV-1 TAR RNA: the target of molecular interactions between the virus and its host.". Curr. HIV Res. 3 (1): 61–71. doi:10.2174/1570162052772924. PMID 15638724. 
  • Le Rouzic E, Benichou S (2006). "The Vpr protein from HIV-1: distinct roles along the viral life cycle.". Retrovirology 2: 11. doi:10.1186/1742-4690-2-11. PMC 554975. PMID 15725353. 
  • Gibellini D, Vitone F, Schiavone P, Re MC (2005). "HIV-1 tat protein and cell proliferation and survival: a brief review.". New Microbiol. 28 (2): 95–109. PMID 16035254. 
  • Hetzer C, Dormeyer W, Schnölzer M, Ott M (2006). "Decoding Tat: the biology of HIV Tat posttranslational modifications.". Microbes Infect. 7 (13): 1364–9. doi:10.1016/j.micinf.2005.06.003. PMID 16046164. 
  • Peruzzi F (2006). "The multiple functions of HIV-1 Tat: proliferation versus apoptosis.". Front. Biosci. 11: 708–17. doi:10.2741/1829. PMID 16146763. 

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